ADVANCED GLYCATION END PRODUCTS (AGES): IS THE SCIENTIFIC NEED TO TRAVEL BACK IN TIME TO REGAIN HEALTH NOW OBVIOUS?

2021 ◽  
pp. 20-22
Author(s):  
Pradeep Kumar Radhakrishnan ◽  
Roshini Ambat ◽  
Gayathri Ananyajyothi Ambat ◽  
Bindu R Nayar ◽  
Y A Nazer
Keyword(s):  
Extracellular Matrix ◽  
Advanced Glycation End Products ◽  
Target Genes ◽  
Cell Types ◽  
Nuclear Factor Κb ◽  
Cooking Methods ◽  
Advanced Glycation ◽  
Surface Receptors ◽  
Glycation End Products ◽  
End Products

Advanced glycation end products (AGEs) are proteins or lipids that become glycated after exposure to sugars. AGEs may modify the extracellular matrix (ECM); modify the action of hormones, cytokines, and free radicals via engagement of cell surface receptors; and impact the function of intracellular proteins..AGEs block nitric oxide activity in the endothelium and cause the production of reactive oxygen species. AGEs cause microvascular and macrovascular complications by formation of cross-links between molecules in the basement membrane of the extracellular matrix and by engaging the receptor for advanced glycation end products (RAGE). Activation of RAGE by AGEs causes upregulation of the transcription factor nuclear factor-κB and its target genes. AGEs can be formed either endogenously or exogenously. Endogenously, advanced glycation takes place in all cell types via the Maillard reaction between reducing sugars and amino residues present in proteins, lipids, and DNA, resulting in loss of protein structure and function followed in some instances by cellular apoptosis. Transition to plant based antioxidant diet with traditional Indian cooking methods seems to confer multitude of health benets.

Stimulation of erythroleukaemia cell differentiation by extracellular high-mobility group-box protein 1 is independent of the receptor for advanced glycation end-products

2002 ◽  
Vol 363 (3) ◽  
pp. 529-535 ◽  
Author(s):  
Bianca SPARATORE ◽  
Marco PEDRAZZI ◽  
Mario PASSALACQUA ◽  
Deborah GAGGERO ◽  
Mauro PATRONE ◽  
...  
Keyword(s):  
Cell Differentiation ◽  
Advanced Glycation End Products ◽  
High Mobility ◽  
Cell Types ◽  
Dominant Negative ◽  
High Mobility Group ◽  
Advanced Glycation ◽  
Stable Transfectants ◽  
Glycation End Products ◽  
End Products

In several cell types the binding of extracellular high-mobility group-box protein 1 (HMGB1) with the receptor for advanced glycation end-products (RAGE) induces cytoskeletal reorganization and cell motility. To establish whether RAGE is also involved in murine erythroleukaemia (MEL) cell differentiation stimulated by HMGB1, we have demonstrated that these cells express a 51kDa protein identified as RAGE, and then we have produced stable transfectants overexpressing wild-type (wt) RAGE or a dominant negative (dn) RAGE mutant lacking the cytoplasmic domain to analyse the differentiation process in these cells. Several experimental findings indicated that RAGE was not involved in the MEL cell differentiation programme. This was also supported by the identical stimulatory effect exerted by HMGB1 on both wt- or dn-RAGE transfectants. We have also observed that HMGB1 binds a 65kDa protein on the surface of MEL cells, supporting the hypothesis that alternative targets of HMGB1 are expressed on the MEL cell membrane and may be involved as mediators of its signalling.

scholarly journals Advanced Glycation End-Products Suppress Mitochondrial Function and Proliferative Capacity of Achilles Tendon-Derived Fibroblasts

2019 ◽  
Author(s):  
Shivam H. Patel ◽  
Feng Yue ◽  
Shannon K. Saw ◽  
Rachel Foguth ◽  
Jason R. Cannon ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Achilles Tendon ◽  
Advanced Glycation End Products ◽  
Mitochondrial Function ◽  
Diabetic Patients ◽  
Proliferative Capacity ◽  
Advanced Glycation ◽  
Tendon Degeneration ◽  
Glycation End Products ◽  
End Products

AbstractDebilitating cases of tendon pain and degeneration affect the majority of diabetic individuals. The high rate of tendon degeneration persists even when glucose levels are well controlled, suggesting that other mechanisms may drive tendon degeneration in diabetic patients. The purpose of this study was to investigate the impact of advanced glycation end-products on tendon fibroblasts to further our mechanistic understanding of the development and progression of diabetic tendinopathy. We proposed that advanced glycation end-products would induce limitations to mitochondrial function and proliferative capacity in tendon-derived fibroblasts, restricting their ability to maintain biosynthesis of tendon extracellular matrix. Using an in-vitro cell culture system, rat Achilles tendon fibroblasts were treated with glycolaldehyde-derived advanced glycation end-products (0, 50, 100, and 200μg/ml) for 48 hours in normal glucose (5.5mM) and high glucose (25mM) conditions. We demonstrate that tendon fibroblasts treated with advanced glycation end-products display reduced ATP production, electron transport efficiency, and proliferative capacity. These impairments were coupled with alterations in mitochondrial DNA content and expression of genes associated with extracellular matrix remodeling, mitochondrial energy metabolism, and apoptosis. Our findings suggest that advanced glycation end-products disrupt tendon fibroblast homeostasis and may be involved in the development and progression of diabetic tendinopathy.

scholarly journals Advanced Glycation End Products and Risks for Chronic Diseases: Intervening Through Lifestyle Modification

2017 ◽  
Vol 13 (4) ◽  
pp. 384-404 ◽  
Author(s):  
Chandan Prasad ◽  
Kathleen E. Davis ◽  
Victorine Imrhan ◽  
Shanil Juma ◽  
Parakat Vijayagopal
Keyword(s):  
Advanced Glycation End Products ◽  
Chemical Nature ◽  
Lifestyle Modification ◽  
Cell Types ◽  
Advanced Glycation ◽  
Disease States ◽  
Multiple Receptors ◽  
Lifestyle Choices ◽  
Glycation End Products ◽  
End Products

Advanced glycation end products (AGEs) are a family of compounds of diverse chemical nature that are the products of nonenzymatic reactions between reducing sugars and proteins, lipids, or nucleic acids. AGEs bind to one or more of their multiple receptors (RAGE) found on a variety of cell types and elicit an array of biologic responses. In this review, we have summarized the data on the nature of AGEs and issues associated with their measurements, their receptors, and changes in their expression under different physiologic and disease states. Last, we have used this information to prescribe lifestyle choices to modulate AGE-RAGE cycle for better health.

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